Dde Biotin Picolyl Azide

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Price (USD)
5 mg
In stock
10 mg
In stock
100 mg
In stock

Dde Biotin Azide Azide is an azide-activated cleavable biotin probe that allows for efficient recovery of avidin-bound protein complexes in affinity-based assays. This reagent contains a biotin moiety linked to azide group through a spacer arm containing a hydrazine-cleavable Dde moiety. Under mild conditions (2% aqueous hydrazine), the Dde liner is cleaved, releasing the biotin tag and any avidin conjugate bound to it.

Molecular weight
Molecular weight left behind
Chemical composition
DMSO, DMF, THF, DCM, Chloroform
Oil to amorphous solid
Storage conditions
Shipping conditions
Ambient temperature

Dde Biotin Picolyl Azide is a unique cleavable biotin probe that allows for release of the captured biomolecules from streptavidin under mild conditions. This reagent contains a biotin moiety linked to picolyl azide group through a spacer arm containing a hydrazine-cleavable Dde moiety. Captured biomolecules can be efficiently released, typically >90% with 2% hydrazine in aqueous media.

Dde Biotin Picolyl Azide incorporates a copper-chelating motif that dramatically accelerates the Cu(I)-catalyzed azide−alkyne cycloaddition (CuAAC) reaction under conditions relevant to biomolecular labeling. Discovery of azides with an internal Cu(I)-chelating motif greatly enhances the utility of CuAAC reaction for monitoring the dynamic glycan biosynthesis in living organisms, the sensitive detection of metabolically labeled proteins DNAs and RNAs, and for many other application where rate acceleration and reduced cell toxicity are highly desirable.

1. Jiang, H., et al. (2014). Monitoring Dynamic Glycosylation in Vivo Using Supersensitive Click Chemistry. Bioconjugate Chem., 25: 698-706. [PubMed]

2. Uttamapinant, C., et al. (2012). Fast, Cell-Compatible Click Chemistry with Copper-Chelating Azides for Biomolecular Labeling. Angew. Chem. Int. Ed,. 51: 5852–56. [PubMed]

3. Yang Y., et al. (2013). Cleavable Trifunctional Biotin Reagents for Protein Labeling, Capture, and Release. Chem. Commun., 48: 5366-86. [PubMed]

4. Matthew E. G., et al. (2017). Comprehensive Mapping of O-GlcNAc Modification Sites Using a Chemically Cleavable Tag. Mol. Biosyst, 12: 1756–59. [PubMed]

5. Gertsik N., et al. (2017). Mapping the Binding Site of BMS-708163 on y-Secretase with Cleavable Photoprobes. Cell Chemical Biology, 32: 3-8. [PubMed]

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